PTPRB_HUMAN - dbPTM
PTPRB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTPRB_HUMAN
UniProt AC P23467
Protein Name Receptor-type tyrosine-protein phosphatase beta
Gene Name PTPRB
Organism Homo sapiens (Human).
Sequence Length 1997
Subcellular Localization Membrane
Single-pass type I membrane protein .
Protein Description Plays an important role in blood vessel remodeling and angiogenesis. Not necessary for the initial formation of blood vessels, but is essential for their maintenance and remodeling. Can induce dephosphorylation of TEK/TIE2, CDH5/VE-cadherin and KDR/VEGFR-2. Regulates angiopoietin-TIE2 signaling in endothelial cells. Acts as a negative regulator of TIE2, and controls TIE2 driven endothelial cell proliferation, which in turn affects blood vessel remodeling during embryonic development and determines blood vessel size during perinatal growth. Essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells and this requires the presence of plakoglobin (By similarity)..
Protein Sequence MLSHGAGLALWITLSLLQTGLAEPERCNFTLAESKASSHSVSIQWRILGSPCNFSLIYSSDTLGAALCPTFRIDNTTYGCNLQDLQAGTIYNFRIISLDEERTVVLQTDPLPPARFGVSKEKTTSTSLHVWWTPSSGKVTSYEVQLFDENNQKIQGVQIQESTSWNEYTFFNLTAGSKYNIAITAVSGGKRSFSVYTNGSTVPSPVKDIGISTKANSLLISWSHGSGNVERYRLMLMDKGILVHGGVVDKHATSYAFHGLTPGYLYNLTVMTEAAGLQNYRWKLVRTAPMEVSNLKVTNDGSLTSLKVKWQRPPGNVDSYNITLSHKGTIKESRVLAPWITETHFKELVPGRLYQVTVSCVSGELSAQKMAVGRTFPDKVANLEANNNGRMRSLVVSWSPPAGDWEQYRILLFNDSVVLLNITVGKEETQYVMDDTGLVPGRQYEVEVIVESGNLKNSERCQGRTVPLAVLQLRVKHANETSLSIMWQTPVAEWEKYIISLADRDLLLIHKSLSKDAKEFTFTDLVPGRKYMATVTSISGDLKNSSSVKGRTVPAQVTDLHVANQGMTSSLFTNWTQAQGDVEFYQVLLIHENVVIKNESISSETSRYSFHSLKSGSLYSVVVTTVSGGISSRQVVVEGRTVPSSVSGVTVNNSGRNDYLSVSWLLAPGDVDNYEVTLSHDGKVVQSLVIAKSVRECSFSSLTPGRLYTVTITTRSGKYENHSFSQERTVPDKVQGVSVSNSARSDYLRVSWVHATGDFDHYEVTIKNKNNFIQTKSIPKSENECVFVQLVPGRLYSVTVTTKSGQYEANEQGNGRTIPEPVKDLTLRNRSTEDLHVTWSGANGDVDQYEIQLLFNDMKVFPPFHLVNTATEYRFTSLTPGRQYKILVLTISGDVQQSAFIEGFTVPSAVKNIHISPNGATDSLTVNWTPGGGDVDSYTVSAFRHSQKVDSQTIPKHVFEHTFHRLEAGEQYQIMIASVSGSLKNQINVVGRTVPASVQGVIADNAYSSYSLIVSWQKAAGVAERYDILLLTENGILLRNTSEPATTKQHKFEDLTPGKKYKIQILTVSGGLFSKEAQTEGRTVPAAVTDLRITENSTRHLSFRWTASEGELSWYNIFLYNPDGNLQERAQVDPLVQSFSFQNLLQGRMYKMVIVTHSGELSNESFIFGRTVPASVSHLRGSNRNTTDSLWFNWSPASGDFDFYELILYNPNGTKKENWKDKDLTEWRFQGLVPGRKYVLWVVTHSGDLSNKVTAESRTAPSPPSLMSFADIANTSLAITWKGPPDWTDYNDFELQWLPRDALTVFNPYNNRKSEGRIVYGLRPGRSYQFNVKTVSGDSWKTYSKPIFGSVRTKPDKIQNLHCRPQNSTAIACSWIPPDSDFDGYSIECRKMDTQEVEFSRKLEKEKSLLNIMMLVPHKRYLVSIKVQSAGMTSEVVEDSTITMIDRPPPPPPHIRVNEKDVLISKSSINFTVNCSWFSDTNGAVKYFTVVVREADGSDELKPEQQHPLPSYLEYRHNASIRVYQTNYFASKCAENPNSNSKSFNIKLGAEMESLGGKCDPTQQKFCDGPLKPHTAYRISIRAFTQLFDEDLKEFTKPLYSDTFFSLPITTESEPLFGAIEGVSAGLFLIGMLVAVVALLICRQKVSHGRERPSARLSIRRDRPLSVHLNLGQKGNRKTSCPIKINQFEGHFMKLQADSNYLLSKEYEELKDVGRNQSCDIALLPENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDSLYYGDLILQMLSESVLPEWTIREFKICGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVLRARKLRSEQENPLFPIYENVNPEYHRDPVYSRH
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
3Phosphorylation-----MLSHGAGLAL
-----CCCCHHHHHH		31.5622496350
28N-linked_GlycosylationLAEPERCNFTLAESK
CCCCHHCCEEEEECC		38.88UniProtKB CARBOHYD
53N-linked_GlycosylationRILGSPCNFSLIYSS
EECCCCCCEEEEECC		32.69UniProtKB CARBOHYD
62PhosphorylationSLIYSSDTLGAALCP
EEEECCCCCCCCCCC		29.10-
72 (in isoform 3)Phosphorylation-37.5230631047
74 (in isoform 3)Phosphorylation-42.0130631047
75N-linked_GlycosylationCPTFRIDNTTYGCNL
CCEEEECCCCEEECC		31.76UniProtKB CARBOHYD
79 (in isoform 3)Phosphorylation-7.5524719451
161 (in isoform 3)Phosphorylation-58.58-
162 (in isoform 3)Phosphorylation-16.03-
172N-linked_GlycosylationWNEYTFFNLTAGSKY
CCEEEEEEEECCCEE		32.08UniProtKB CARBOHYD
198N-linked_GlycosylationRSFSVYTNGSTVPSP
CEEEEEECCCCCCCC		25.40UniProtKB CARBOHYD
200 (in isoform 3)Phosphorylation-28.44-
201PhosphorylationSVYTNGSTVPSPVKD
EEEECCCCCCCCCCC		37.52-
204PhosphorylationTNGSTVPSPVKDIGI
ECCCCCCCCCCCCCC		37.68-
204 (in isoform 3)Phosphorylation-37.68-
205 (in isoform 3)Phosphorylation-30.98-
267N-linked_GlycosylationLTPGYLYNLTVMTEA
CCCCCEEEEEEEECC		27.00UniProtKB CARBOHYD
287PhosphorylationYRWKLVRTAPMEVSN
CCEEEEEECCEEEEC		27.8622210691
293PhosphorylationRTAPMEVSNLKVTND
EECCEEEECEEEECC		24.1229978859
298PhosphorylationEVSNLKVTNDGSLTS
EEECEEEECCCCEEE		26.4629978859
302PhosphorylationLKVTNDGSLTSLKVK
EEEECCCCEEEEEEE		31.1929978859
304PhosphorylationVTNDGSLTSLKVKWQ
EECCCCEEEEEEEEC		33.4429978859
305PhosphorylationTNDGSLTSLKVKWQR
ECCCCEEEEEEEECC		31.3322210691
321N-linked_GlycosylationPGNVDSYNITLSHKG
CCCCCEEEEEEEECC		25.40UniProtKB CARBOHYD
414N-linked_GlycosylationQYRILLFNDSVVLLN
HEEEEEECCEEEEEE		40.39UniProtKB CARBOHYD
421N-linked_GlycosylationNDSVVLLNITVGKEE
CCEEEEEEEEECCCC		24.59UniProtKB CARBOHYD
465PhosphorylationSERCQGRTVPLAVLQ
CCCCCCCCCCEEEEE		33.04-
479N-linked_GlycosylationQLRVKHANETSLSIM
EEEEECCCCCCEEEE		53.44UniProtKB CARBOHYD
512PhosphorylationDLLLIHKSLSKDAKE
CEEEEECCCCCCCCC		24.5824247654
514PhosphorylationLLIHKSLSKDAKEFT
EEEECCCCCCCCCCC		35.2624247654
531PhosphorylationDLVPGRKYMATVTSI
CCCCCCEEEEEEEEE		7.2218452278
534PhosphorylationPGRKYMATVTSISGD
CCCEEEEEEEEEECC		14.0518452278
537PhosphorylationKYMATVTSISGDLKN
EEEEEEEEEECCCCC		15.4918452278
539PhosphorylationMATVTSISGDLKNSS
EEEEEEEECCCCCCC		26.48-
544N-linked_GlycosylationSISGDLKNSSSVKGR
EEECCCCCCCCCCCC		55.19UniProtKB CARBOHYD
574N-linked_GlycosylationMTSSLFTNWTQAQGD
CCCCHHCCCCCCCCC		32.25UniProtKB CARBOHYD
598N-linked_GlycosylationHENVVIKNESISSET
EECEEEECCCCCCCC		36.80UniProtKB CARBOHYD
605PhosphorylationNESISSETSRYSFHS
CCCCCCCCCCEEEEE		22.06-
606PhosphorylationESISSETSRYSFHSL
CCCCCCCCCEEEEEC		25.77-
609PhosphorylationSSETSRYSFHSLKSG
CCCCCCEEEEECCCC		18.5130576142
615PhosphorylationYSFHSLKSGSLYSVV
EEEEECCCCCEEEEE		38.6218785766
624PhosphorylationSLYSVVVTTVSGGIS
CEEEEEEEEEECCCC		15.1830576142
625PhosphorylationLYSVVVTTVSGGISS
EEEEEEEEEECCCCC		10.8918785766
627PhosphorylationSVVVTTVSGGISSRQ
EEEEEEEECCCCCCE		29.2518785766
652N-linked_GlycosylationSVSGVTVNNSGRNDY
CEEEEEECCCCCCCE		27.81UniProtKB CARBOHYD
698PhosphorylationAKSVRECSFSSLTPG
EECCCCCCCCCCCCC		24.34-
701PhosphorylationVRECSFSSLTPGRLY
CCCCCCCCCCCCCEE		33.96-
709PhosphorylationLTPGRLYTVTITTRS
CCCCCEEEEEEEECC		18.76-
711PhosphorylationPGRLYTVTITTRSGK
CCCEEEEEEEECCCC		12.5729759185
713PhosphorylationRLYTVTITTRSGKYE
CEEEEEEEECCCCCC		13.5429759185
714PhosphorylationLYTVTITTRSGKYEN
EEEEEEEECCCCCCC		20.9829759185
719PhosphorylationITTRSGKYENHSFSQ
EEECCCCCCCCCCCC		26.03-
721N-linked_GlycosylationTRSGKYENHSFSQER
ECCCCCCCCCCCCCC		32.77UniProtKB CARBOHYD
723PhosphorylationSGKYENHSFSQERTV
CCCCCCCCCCCCCCC		37.87-
725PhosphorylationKYENHSFSQERTVPD
CCCCCCCCCCCCCCC		33.86-
738PhosphorylationPDKVQGVSVSNSARS
CCCCCCEEECCCCCC		27.0118785766
740PhosphorylationKVQGVSVSNSARSDY
CCCCEEECCCCCCCE		19.9823898821
742PhosphorylationQGVSVSNSARSDYLR
CCEEECCCCCCCEEE		19.9723898821
777PhosphorylationNNFIQTKSIPKSENE
CCEEEECCCCCCCCC		47.7322210691
829N-linked_GlycosylationVKDLTLRNRSTEDLH
CCCCCCCCCCCCCEE		45.42UniProtKB CARBOHYD
1008PhosphorylationVIADNAYSSYSLIVS
EECCCCCCCEEEEEE		22.01-
1026PhosphorylationAAGVAERYDILLLTE
HCCHHHHCCEEEEEC		9.9924114839
1032PhosphorylationRYDILLLTENGILLR
HCCEEEEECCCEEEE		27.6324114839
1040N-linked_GlycosylationENGILLRNTSEPATT
CCCEEEECCCCCCCC		48.18UniProtKB CARBOHYD
1067PhosphorylationKYKIQILTVSGGLFS
EEEEEEEEEECCCCC		17.7914729942
1069PhosphorylationKIQILTVSGGLFSKE
EEEEEEEECCCCCHH		23.1614729942
1074PhosphorylationTVSGGLFSKEAQTEG
EEECCCCCHHCCCCC		34.3324719451
1079PhosphorylationLFSKEAQTEGRTVPA
CCCHHCCCCCCCCCC		47.6726074081
1083PhosphorylationEAQTEGRTVPAAVTD
HCCCCCCCCCCEEEE		41.5226074081
1089PhosphorylationRTVPAAVTDLRITEN
CCCCCEEEEEEECCC		25.2926074081
1096N-linked_GlycosylationTDLRITENSTRHLSF
EEEEECCCCCEEEEE		39.78UniProtKB CARBOHYD
1163N-linked_GlycosylationTHSGELSNESFIFGR
EECCCCCCCEEECCC		62.65UniProtKB CARBOHYD
1177PhosphorylationRTVPASVSHLRGSNR
CEECCCHHHHCCCCC		17.8224719451
1185N-linked_GlycosylationHLRGSNRNTTDSLWF
HHCCCCCCCCCCCEE		52.13UniProtKB CARBOHYD
1195PhosphorylationDSLWFNWSPASGDFD
CCCEECCCCCCCCCC		16.22-
1209PhosphorylationDFYELILYNPNGTKK
CEEEEEEECCCCCCC		22.91-
1212N-linked_GlycosylationELILYNPNGTKKENW
EEEEECCCCCCCCCC		68.10UniProtKB CARBOHYD
1246PhosphorylationVLWVVTHSGDLSNKV
EEEEEEECCCCCCCE		25.3327251275
1250PhosphorylationVTHSGDLSNKVTAES
EEECCCCCCCEEECC		39.0722210691
1274N-linked_GlycosylationMSFADIANTSLAITW
HHHHHHCCCCEEEEE		30.45UniProtKB CARBOHYD
1314PhosphorylationNPYNNRKSEGRIVYG
CCCCCCCCCCEEEEE		41.8827251275
1320PhosphorylationKSEGRIVYGLRPGRS
CCCCEEEEECCCCCE		14.2027251275
1328PhosphorylationGLRPGRSYQFNVKTV
ECCCCCEEEEEEEEE		18.7627251275
1350PhosphorylationYSKPIFGSVRTKPDK
CCCCCCCCCCCCCHH		9.5530177828
1353PhosphorylationPIFGSVRTKPDKIQN
CCCCCCCCCCHHCCC		44.7830177828
1367N-linked_GlycosylationNLHCRPQNSTAIACS
CEEECCCCCCCEEEE		43.97UniProtKB CARBOHYD
1421PhosphorylationMLVPHKRYLVSIKVQ
HHCCCCEEEEEEEEE		19.0920049867
1440PhosphorylationTSEVVEDSTITMIDR
CCEEEECCEEEEECC		14.2722210691
1441PhosphorylationSEVVEDSTITMIDRP
CEEEECCEEEEECCC		32.5622210691
1443PhosphorylationVVEDSTITMIDRPPP
EEECCEEEEECCCCC		14.2522210691
1470N-linked_GlycosylationLISKSSINFTVNCSW
EEECCEEEEEEEEEE		28.60UniProtKB CARBOHYD
1474N-linked_GlycosylationSSINFTVNCSWFSDT
CEEEEEEEEEEEECC		15.85UniProtKB CARBOHYD
1518N-linked_GlycosylationSYLEYRHNASIRVYQ
CHHHHHHCCEEEEEE		26.78UniProtKB CARBOHYD
1554PhosphorylationKLGAEMESLGGKCDP
EECHHHHHCCCCCCH		30.8818785766
1647PhosphorylationLICRQKVSHGRERPS
HHHHHHHHCCCCCCC		27.5317081983
1654PhosphorylationSHGRERPSARLSIRR
HCCCCCCCCCEEECC		32.0424501219
1658PhosphorylationERPSARLSIRRDRPL
CCCCCCEEECCCCCE		14.4328978645
1666PhosphorylationIRRDRPLSVHLNLGQ
ECCCCCEEEEEECCC		15.3523403867
1699PhosphorylationFMKLQADSNYLLSKE
EEEEECCCCCHHCHH		30.3227732954
1701PhosphorylationKLQADSNYLLSKEYE
EEECCCCCHHCHHHH		16.9927732954
1704PhosphorylationADSNYLLSKEYEELK
CCCCCHHCHHHHHHH		22.3527732954
1705UbiquitinationDSNYLLSKEYEELKD
CCCCHHCHHHHHHHH		65.37-
1733PhosphorylationENRGKNRYNNILPYD
CCCCCCCCCCCCCCC		23.19-
1739PhosphorylationRYNNILPYDATRVKL
CCCCCCCCCCCEEEE		18.11-
1742PhosphorylationNILPYDATRVKLSNV
CCCCCCCCEEEECCC		32.85-
1953PhosphorylationMVQTECQYVYLHQCV
EEECCCCHHHHHHHH		11.61-
1955PhosphorylationQTECQYVYLHQCVRD
ECCCCHHHHHHHHHH		8.11-
1981PhosphorylationENPLFPIYENVNPEY
CCCCCCCCCCCCHHH		11.1623403867
1988PhosphorylationYENVNPEYHRDPVYS
CCCCCHHHCCCCCCC		11.9226356563
1994PhosphorylationEYHRDPVYSRH----
HHCCCCCCCCC----		12.84-
1995PhosphorylationYHRDPVYSRH-----
HCCCCCCCCC-----		24.9027134283
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PTPRB_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTPRB_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PTPRB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MAGI3_HUMANMAGI3physical
12615970
CADH5_HUMANCDH5physical
12234928
CNTN1_HUMANCNTN1physical
7628014
EGFR_HUMANEGFRphysical
8870675
VEGFA_HUMANVEGFAphysical
25644401
PTN_HUMANPTNphysical
25644401
RABE2_HUMANRABEP2physical
27880917
GOPC_HUMANGOPCphysical
27880917
PTPRG_HUMANPTPRGphysical
27880917
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PTPRB_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1647, AND MASSSPECTROMETRY.
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry.";
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.;
Anal. Chem. 76:2763-2772(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1067 AND SER-1069, ANDMASS SPECTROMETRY.

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